ID A0A0F2N2S2_9FIRM Unreviewed; 384 AA.
AC A0A0F2N2S2;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Peptidase S1 {ECO:0000313|EMBL:KJR96287.1};
GN ORFNames=VR68_14665 {ECO:0000313|EMBL:KJR96287.1};
OS Peptococcaceae bacterium BRH_c4a.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae.
OX NCBI_TaxID=1629716 {ECO:0000313|EMBL:KJR96287.1, ECO:0000313|Proteomes:UP000033439};
RN [1] {ECO:0000313|EMBL:KJR96287.1, ECO:0000313|Proteomes:UP000033439}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BRH_c4a {ECO:0000313|EMBL:KJR96287.1};
RA Bagnoud A., Chourey K., Hettich R.L., de Bruijn I., Andersson A.F.,
RA Leupin O.X., Schwyn B., Bernier-Latmani R.;
RT "Microbial metabolic network in the subsurface.";
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S1C family.
CC {ECO:0000256|ARBA:ARBA00010541}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KJR96287.1}.
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DR EMBL; LADN01000088; KJR96287.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F2N2S2; -.
DR STRING; 1629716.VR68_14665; -.
DR PATRIC; fig|1629716.3.peg.83; -.
DR Proteomes; UP000033439; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00987; PDZ_serine_protease; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001940; Peptidase_S1C.
DR PANTHER; PTHR22939; SERINE PROTEASE FAMILY S1C HTRA-RELATED; 1.
DR PANTHER; PTHR22939:SF129; SERINE PROTEASE HTRA2, MITOCHONDRIAL; 1.
DR Pfam; PF13180; PDZ_2; 1.
DR Pfam; PF13365; Trypsin_2; 1.
DR PRINTS; PR00834; PROTEASES2C.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS50106; PDZ; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 276..336
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
SQ SEQUENCE 384 AA; 40541 MW; 582D58321B0217E8 CRC64;
MNPGKEKNKA AIFIIAAFVV GVLVTGAAFY LLPILQSTAT LQNTGSNPPI QAGTEVIAGI
VEKTSPAVVL IQTSVESKSR SYDPFFNDPF FRDFFGGRVP MDSGPRVSRG MGSGFIISKE
GYILTNEHVI SGAKKIEVII TGKDKPVPAK LVGSDFELDL AVLKINSEGD LPTLELGDSD
AVRVGEWTIA IGNPQGLDHT VTVGVISAKG RPVSVQDRNY KNLLQTDASI NPGNSGGPLL
NTGGQVIGIN TAVNASAQGI GFAIPTSTVR PVLDTLINQG KITRPWMGVY IQTVNKEISD
YLKLGSTEGV LVTSVVERGP ADTAGITQGD VITEINQGKV ANASDLTDLI RKMKPGQKTM
VVVYRGGQKL LVEVTIGEKG KIEG
//
